› 5uhp

X-ray diffraction
2.79Å resolution

Crystal structure of the core catalytic domain of human O-GlcNAcase

Released:
DOI: 10.2210/pdb5uhp/pdb
PDB entry 5uhp coloured by chain, front view.
PDB entry 5uhp coloured by chain, side view.
PDB entry 5uhp coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Klein DJ, Elsen NL

Function and Biology Details

Reaction catalysed: 
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130002 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein O-GlcNAcase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 388 amino acids
Theoretical weight: 43.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O60502 (Residues: 14-400; Coverage: 42%)
Gene names: HEXC, KIAA0679, MEA5, MGEA5, OGA
Sequence domains: beta-N-acetylglucosaminidase
Structure domains: Glycosidases
Protein O-GlcNAcase Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 161 amino acids
Theoretical weight: 18.76 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O60502 (Residues: 553-705; Coverage: 17%)
Gene names: HEXC, KIAA0679, MEA5, MGEA5, OGA

Ligands and Environments

1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 89.722Å b: 91.531Å c: 94.517Å
α: 77.27° β: 62.81° γ: 63.03°
R-values:
R R work R free
0.242 0.239 0.292
Expression system: Spodoptera frugiperda

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